SAXSdb — 1e8o

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1. Protein Identity and Related Structures Protein Identity & Related Structures

SIGNAL RECOGNITION PARTICLE 9 KDA PROTEIN

HOMO SAPIENS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–RNA	Heteromer	Protein 4 RNA 1	SIGNAL RECOGNITION PARTICLE 14 KDA PROTEIN × 2 （P37108） 7SL RNA × 1 SULFATE ION × 3 water × 5	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SR09_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–85； UniProt 1–85 Author chain C； PDBConstruct 1–85； UniProt 1–85

SIGNAL RECOGNITION PARTICLE 14 KDA PROTEIN

HOMO SAPIENS

UniProt P37108

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–RNA	Heteromer	Protein 4 RNA 1	SIGNAL RECOGNITION PARTICLE 9 KDA PROTEIN × 2 （P49458） 7SL RNA × 1 SULFATE ION × 3 water × 5	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SR14_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–106； UniProt 2–107 Author chain D； PDBConstruct 1–106； UniProt 2–107

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1e8o
Deposition date deposition_date	2000-09-28
Structure title title	Core of the Alu domain of the mammalian SRP
Keywords keywords	;ALU RIBONUCLEOPROTEIN PARTICLE, PROTEIN RECOGNITION OF AN RNA U-TURN, TRANSLATIONAL CONTROL, ALU RNP ASSEMBLY AND TRANSPORT, ALU RETROPOSITION ;; ALU RIBONUCLEOPROTEIN PARTICLE
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1e8o__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1e8o__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1e8o__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	27.66 Å
Rg (electron density)	29.05 Å
Total Rg	29.48 Å
Atom count	3486
Residues	345
Excluded volume	58622 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1e8o__assembly_1__model_1`	pentameric （5）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	SIGNAL RECOGNITION PARTICLE 9 KDA PROTEIN
Molecular weight formula_weight	9996.6 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	3508

PQYQTWEEFSRAAEKLYLADPMKARVVLKYRHSDGNLCVKVTDDLVCLVYKTDQAQDVKKIEKFHSQLMRLMVAKEARNVTMETE

Source Source

Source organism organism	HOMO SAPIENS
Common name common_name	HUMAN
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	SIGNAL RECOGNITION PARTICLE 14 KDA PROTEIN
Molecular weight formula_weight	12114.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

VLLESEQFLTELTRLFQKCRTSGSVYITLKKYDGRTKPIPKKGTVEGFEPADNKCLLRATDGKKKISTVVSSKEVNKFQMAYSNLLRANMDGLKKRDKKNKTKKTK

Source Source

Source organism organism	HOMO SAPIENS
Common name common_name	HUMAN
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 polymer

Description description	7SL RNA
Molecular weight formula_weight	16277.6 kDa
Mutation mutation	YES
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polyribonucleotide
Chain IDs strand_id	E

GGGCCGGGCGCGGUGGCGCGCGCCUGUAGUCCCAGCUACUCGGGAGGCUC

Entity 4 Entity 4 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	22

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1e8oa_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.49 — Signal recognition particle alu RNA binding heterodimer, SRP9/14
Superfamily Superfamily superfamily	d.49.1 — Signal recognition particle alu RNA binding heterodimer, SRP9/14
Family Family family	d.49.1.1 — Signal recognition particle alu RNA binding heterodimer, SRP9/14

Domain ID domain_id	d1e8ob_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.49 — Signal recognition particle alu RNA binding heterodimer, SRP9/14
Superfamily Superfamily superfamily	d.49.1 — Signal recognition particle alu RNA binding heterodimer, SRP9/14
Family Family family	d.49.1.1 — Signal recognition particle alu RNA binding heterodimer, SRP9/14

Domain ID domain_id	d1e8oc_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.49 — Signal recognition particle alu RNA binding heterodimer, SRP9/14
Superfamily Superfamily superfamily	d.49.1 — Signal recognition particle alu RNA binding heterodimer, SRP9/14
Family Family family	d.49.1.1 — Signal recognition particle alu RNA binding heterodimer, SRP9/14

Domain ID domain_id	d1e8od_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.49 — Signal recognition particle alu RNA binding heterodimer, SRP9/14
Superfamily Superfamily superfamily	d.49.1 — Signal recognition particle alu RNA binding heterodimer, SRP9/14
Family Family family	d.49.1.1 — Signal recognition particle alu RNA binding heterodimer, SRP9/14

CATH v4.4 (4 domains)

Domain ID domain_id	1e8oA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	720 — Signal recognition particle alu RNA binding heterodimer, srp9/1
Homologous superfamily homologous superfamily	10 — Signal recognition particle alu RNA binding heterodimer, srp9/1

Domain ID domain_id	1e8oB00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	720 — Signal recognition particle alu RNA binding heterodimer, srp9/1
Homologous superfamily homologous superfamily	10 — Signal recognition particle alu RNA binding heterodimer, srp9/1

Domain ID domain_id	1e8oC00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	720 — Signal recognition particle alu RNA binding heterodimer, srp9/1
Homologous superfamily homologous superfamily	10 — Signal recognition particle alu RNA binding heterodimer, srp9/1

Domain ID domain_id	1e8oD00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	720 — Signal recognition particle alu RNA binding heterodimer, srp9/1
Homologous superfamily homologous superfamily	10 — Signal recognition particle alu RNA binding heterodimer, srp9/1

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Unit-cell length a length_a	57.448 Å
Unit-cell length b length_b	186.621 Å
Unit-cell length c length_c	189.824 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	3.200 Å
Low-resolution limit resolution_low	47.460 Å
R factor r_factor	0.2450
R_work r_work	0.2450
R_free r_free	0.2910

Core of the Alu domain of the mammalian SRP

1. Protein Identity and Related Structures Protein Identity & Related Structures

SIGNAL RECOGNITION PARTICLE 9 KDA PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

SIGNAL RECOGNITION PARTICLE 14 KDA PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1e8o__assembly_1__model_1

1e8o__assembly_1__model_1 | I(q)

1e8o__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Core of the Alu domain of the mammalian SRP

1. Protein Identity and Related Structures Protein Identity & Related Structures

SIGNAL RECOGNITION PARTICLE 9 KDA PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

SIGNAL RECOGNITION PARTICLE 14 KDA PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1e8o__assembly_1__model_1

1e8o__assembly_1__model_1 | I(q)

1e8o__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)